Figure 3
NMR data for [ U -15N]-labeled HscB in the presence of a six-fold molar excess of apo-IscU. Combined chemical shift changes (ΔδHNIscU) are plotted for wild-type HscB (black), HscB(D103A) (yellow), HscB(E100A) (green), and HscB(L96A) (red). ΔδHNIscU values are reported as the combination of changes in the proton (ΔδHIscU) and nitrogen (ΔδNIscU) dimensions according to ΔδHNIscU = [(ΔδHIscU)2 + ΔδNIscU/6)2]1/2 [29]. ΔδHIscU and ΔδNIscU are calculated relative to the free form of each protein. Residues whose peaks disappear in the presence of apo-IscU for at least one form of HscB are marked with an asterisk and are also listed in Additional Files 5 to 8. Values are not shown for residues that have an unassigned 1HN-15N cross-peak in free HscB, that lack an observable 1H-15N cross-peak in free and/or bound HscB, have an overlapped 1H-15N cross-peak in free and/or bound HscB, or are prolines (P10, P33, and P64). The diagram at the top of each panel shows the location of secondary structural elements in E. coli HscB.